GenomeNet

Database: UniProt
Entry: A4XA26_SALTO
LinkDB: A4XA26_SALTO
Original site: A4XA26_SALTO 
ID   A4XA26_SALTO            Unreviewed;       474 AA.
AC   A4XA26;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN   OrderedLocusNames=Strop_3332 {ECO:0000313|EMBL:ABP55766.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS   105044 / CNB-440).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP55766.1, ECO:0000313|Proteomes:UP000000235};
RN   [1] {ECO:0000313|Proteomes:UP000000235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC   {ECO:0000313|Proteomes:UP000000235};
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000777,
CC         ECO:0000256|RuleBase:RU004356};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC       ECO:0000256|RuleBase:RU000384}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000667; ABP55766.1; -; Genomic_DNA.
DR   RefSeq; WP_012014543.1; NC_009380.1.
DR   AlphaFoldDB; A4XA26; -.
DR   STRING; 369723.Strop_3332; -.
DR   KEGG; stp:Strop_3332; -.
DR   PATRIC; fig|369723.5.peg.3434; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_1_2_11; -.
DR   OMA; PHPHEFE; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR036651; Gln_synt_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR004809; Gln_synth_I.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   NCBIfam; TIGR00653; GlnA; 1.
DR   PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR43407:SF1; LENGSIN; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW   ECO:0000256|RuleBase:RU004356};
KW   Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:ABP55766.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW   ECO:0000256|RuleBase:RU004356};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|PIRSR:PIRSR604809-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000235}.
FT   DOMAIN          15..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          107..474
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         226..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         267..268
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         274..276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         325
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         331
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         343
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   BINDING         357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT   BINDING         364
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT   MOD_RES         402
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ   SEQUENCE   474 AA;  53460 MW;  531B5687B0B6EE30 CRC64;
     MFANPEELLR YLKNEDVKFV DVRFCDLPGV MQHFNLPAES IDDELLTDGL AFDGSSIRGF
     QAIHESDMLL LPDVATAFID PFRAQKTLAL NFFIHDPFTR EAYSRDPRNV AKKAEAYLAA
     SGIADTAYFG AEAEFYIFDS IRHETSAHQS YYYIDSIEGW WNTGRDEEGG NRGYKTAYKG
     GYFPVPPVDH YADLRDKIVR RMIDAGYTVE RSHHEVGTAG QAEINYKFST LLHAADQLQL
     FKYIVKNETW VNGKTATFMP KPLFGDNGSG MHTHQSLWLN GEPLFYDETG YAGLSDTARW
     YIGGLLQHAP SLLAFTNPTV NSYRRLVPGF EAPVNLVYSQ RNRSACTRIP VTGSNPKAKR
     VEFRVPDPSA NVYLAFSAML MAGLDGIKNK TEPPTPIDKD LYDLPPEEWG DVKQVPGSLP
     AVLDSLEADH DYLLDGGVFT PDLISTWIDW KRTNEVDPVR LRPTPHEFAM YFDC
//
DBGET integrated database retrieval system